7CUP

Structure of 2,5-dihydroxypridine Dioxygenase from Pseudomonas putida KT2440

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0009056	biological_process	catabolic process
A	0016491	molecular_function	oxidoreductase activity
A	0046872	molecular_function	metal ion binding
A	0047075	molecular_function	2,5-dihydroxypyridine 5,6-dioxygenase activity
A	1901848	biological_process	nicotinate catabolic process
B	0009056	biological_process	catabolic process
B	0016491	molecular_function	oxidoreductase activity
B	0046872	molecular_function	metal ion binding
B	0047075	molecular_function	2,5-dihydroxypyridine 5,6-dioxygenase activity
B	1901848	biological_process	nicotinate catabolic process
C	0009056	biological_process	catabolic process
C	0016491	molecular_function	oxidoreductase activity
C	0046872	molecular_function	metal ion binding
C	0047075	molecular_function	2,5-dihydroxypyridine 5,6-dioxygenase activity
C	1901848	biological_process	nicotinate catabolic process
D	0009056	biological_process	catabolic process
D	0016491	molecular_function	oxidoreductase activity
D	0046872	molecular_function	metal ion binding
D	0047075	molecular_function	2,5-dihydroxypyridine 5,6-dioxygenase activity
D	1901848	biological_process	nicotinate catabolic process
E	0009056	biological_process	catabolic process
E	0016491	molecular_function	oxidoreductase activity
E	0046872	molecular_function	metal ion binding
E	0047075	molecular_function	2,5-dihydroxypyridine 5,6-dioxygenase activity
E	1901848	biological_process	nicotinate catabolic process
F	0009056	biological_process	catabolic process
F	0016491	molecular_function	oxidoreductase activity
F	0046872	molecular_function	metal ion binding
F	0047075	molecular_function	2,5-dihydroxypyridine 5,6-dioxygenase activity
F	1901848	biological_process	nicotinate catabolic process

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	18
Details	BINDING: BINDING => ECO:0000255

Chain	Residue	Details
A	HIS265
D	HIS265
D	HIS318
D	ASP320
E	HIS265
E	HIS318
E	ASP320
F	HIS265
F	HIS318
F	ASP320
A	HIS318
A	ASP320
B	HIS265
B	HIS318
B	ASP320
C	HIS265
C	HIS318
C	ASP320

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